Synergistic inhibition of isolated flavonoids from Moringa oleifera leaf on α-glucosidase activity

Hamed, Yahya Saud; Abdin, Mohamed; Rayan, Ahmed M.; Akhtar, Hafiz Muhammad Saleem; Zeng, Xiaoxiong

doi:10.1016/j.lwt.2021.111081

Cited by 26 publications

(27 citation statements)

References 33 publications

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“…Similar phenomena were observed by some previous studies [6,10]. For example, a previous study also found that different flavonoids isolated from Moringa oleifera leaf showed synergistic inhibition on α-glucosidase activity [22]. e interaction results of myricetrin and dihydromyricetin on pancreatic lipase are presented in Table 2.…”

Section: Interaction Of Myricetrin and Dihydromyricetin Onsupporting

confidence: 86%

Inhibitory Effects of Myricetrin and Dihydromyricetin toward α-Glucosidase and Pancreatic Lipase with Molecular Docking Analyses and Their Interaction

Liu

et al. 2021

Journal of Food Quality

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The aim of the current study was to evaluate the interaction effects of myricetrin and dihydromyricetin in inhibiting α-glucosidase and pancreatic lipase at different combination ratios and concentrations and to illuminate the underlying mechanisms of their inhibitions by molecular docking analyses. Results showed that both phenolic compounds possessed good inhibitory effects toward two enzymes in a dose-dependent manner. Myricetrin demonstrated a stronger inhibition against α-glucosidase (IC50, 41.14 ± 2.52 and more than 200 μg/mL, respectively), while dihydromyricetin had a better pancreatic lipase inhibition (IC50, 244.96 ± 4.24 and 373.26 ± 21.36 μg/mL, respectively). Different interaction types were observed when myricetrin and dihydromyricetin inhibited α-glucosidase and pancreatic lipase in combination, which were closely related to the combination ratio and concentration. For α-glucosidase inhibition, synergistic effects were observed at relative low concentrations when the combination ratio of myricetrin to dihydromyricetin was set as 1 : 2, while strong synergistic effects existed at relative high concentrations for pancreatic lipase inhibition. In other combination ratios (1 : 1 or 2 : 1), additive and/or antagonistic effects occurred. Molecular docking analyses showed that myricetrin formed nine hydrogen bonds with α-glucosidase, while only three hydrogen bonds were formed between dihydromyricetin and α-glucosidase. However, these two phenolic compounds had similar hydrogen bonds and hydrophobic interactions with pancreatic lipase. The present study suggested that myricetrin and dihydromyricetin or food materials rich in these two phenolic compounds could be exploited as α-glucosidase and/or pancreatic lipase inhibitors to deal with health problems caused by excessive energy intake, and the combination ratio and concentration of these two phenolic compounds should be considered when producing new functional foods.

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Section: Interaction Of Myricetrin and Dihydromyricetin Onsupporting

confidence: 86%

Inhibitory Effects of Myricetrin and Dihydromyricetin toward α-Glucosidase and Pancreatic Lipase with Molecular Docking Analyses and Their Interaction

Liu

et al. 2021

Journal of Food Quality

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“…Previous studied suggested that flavonoids possessed excellent inhibitory effects on α-glucosidase ( Semaan et al 2018 ). Quercetin derivatives and kaempferol are the most predominant flavonoids in the PCF extract, showing an excellent inhibitory effect on α-glucosidase, α-amylase and lipase, in good agreement with Hamed et al (2021) . From the obtained results, it seems that PCF extract is more effective in inhibiting the lipase, followed by α-amylase , tyrosinase and α-glucosidase.…”

Section: Resultssupporting

confidence: 67%

Optimizing of the extraction conditions for anthocyanin’s from purple corn flour (Zea mays L): Evidences on selected properties of optimized extract

et al. 2023

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“…The bark extract (Figure 2B) exhibits a non-competitive type of inhibition in IC25 (reduce Vmax), but with increased concentration to IC50, the Linewear-Burk plot reveals an uncompetitive inhibition behavior. Uncompetitive inhibitors bind to the enzyme and improve the binding of the substrate (thus, reducing Km), but the resultant enzyme-inhibitor-substrate complex only undergoes a reaction to slowly form the product; thus, Vmax is also reduced (Hamed et al, 2021). Sources: Authors.…”

Section: Inhibition and Inhibition Kinetics Of α-Glucosidasementioning

confidence: 99%

α-Glucosidase inhibitory properties of leaves and bark extracts of Curatella americana L.

Barbosa

Soares

Lacerda

et al. 2022

RSD

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In this article, we investigate the inhibitory activity of methanolic extracts of bark and leaves of Curatella americana L. against α-glucosidase. Furthermore, antioxidant activity was evaluated using DPPH and ABTS assays, and the interaction of the identified compound of the extracts and α-glucosidase was tested by molecular docking. The results show that C. americana has a strong inhibitory activity against α-glucosidase reaching an IC 50 value of 7.29 µg/ml and 7.26 µg/ml for the extracts of bark and leaves, respectively. The enzyme kinetics reveals a mixed competitive mechanism for the leaves extract and an uncompetitive type of inhibition for the bark extract. The results of the antioxidant activity showed that both extracts have great antioxidant capacity, with the leaves extract having a better performance. The identified compounds of the extracts have a high binding affinity to the enzyme. Therefore, the study showed that C. americana extracts have a great potential for the treatment of diabetes, possibly serving as a therapeutic option to treat postprandial hyperglycemia and prevent long-term pathologies associated with diabetes.

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Synergistic inhibition of isolated flavonoids from Moringa oleifera leaf on α-glucosidase activity

Cited by 26 publications

References 33 publications

Inhibitory Effects of Myricetrin and Dihydromyricetin toward α-Glucosidase and Pancreatic Lipase with Molecular Docking Analyses and Their Interaction

Inhibitory Effects of Myricetrin and Dihydromyricetin toward α-Glucosidase and Pancreatic Lipase with Molecular Docking Analyses and Their Interaction

Optimizing of the extraction conditions for anthocyanin’s from purple corn flour (Zea mays L): Evidences on selected properties of optimized extract

α-Glucosidase inhibitory properties of leaves and bark extracts of Curatella americana L.

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